Hi Jahan,
You could also try dehydrating the crystals by moving them over well
solutions of ammonium sulfate, sodium chloride, or high molecular weight
PEG, starting with low concentrations, and slowly increasing over time.
Good luck,
Sara
On Mon, Oct 15, 2012 at 10:06 PM, Raji Edayathumangalam
Hi Jahan,
Since I can't tell what you tried in terms of improving/optimizing
crystallization, here are some methods that my some colleagues and I have
had good luck with, in addition to what Gopal has suggested.
(1) Sitting drop technique under oil
(2) Varying ratios of protein to precipitant
(3)
During optimization, have you tried Hampton's additive screen?
Gopal
From: CCP4 bulletin board [CCP4BB@JISCMAIL.AC.UK] On Behalf Of Jahan Alikhajeh
[ja...@graduate.org]
Sent: Monday, October 15, 2012 6:01 PM
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] Plat
Dear Friends,
I am trying to crystalize a 70 kDa nasty protein but I got plate shape
crystals with high mosaicity and useless diffraction (up to 4A).
I tried to improve/optimize crystallization but either I got the same or
nothing. I tried seeding but I had so many crystals without any improve
Hi Sandra,
Yes, there are several ways of getting this information.
Go to PDB website Advanced Search section. In the Query Type pull down, select
All and then select "Remove Similar Sequences at 30% identity". You will have
to select 30% cut off in the pull down menu. This will result in ~22
Daniel Schectman's 2012 nobel prize for the discovery of quasicrystals is
missing.
On Sat, Oct 13, 2012 at 5:01 PM, Joel Sussman
wrote:
> Just want to make sure anyone interested in Nobel Prizes knows about this
> existing page:
>
> http://proteopedia.org/wiki/index.php/Nobel_Prizes_for_3D_Molec
I am not quite sure I understand your question, but ligands are treated much
the same way as any other moiety. The dictionary lists target distances, angles
etc and the expected SD on these. The default values are chosen according to
the chemical bond type. You should check these - the dictiona
Hi! Does anybody know which is the range is used by REFMAC to vary bond
distances, angles, and torsions of a ligand molecule during a refinement
process? Is it possible to control and choose this range? In which way?
Where are these information in cif dictionary obtained by sketcher in
CCP4?
t
HI! Does anybody know the number or a likely number of unique structures
(solved by Xray) deposited in PDB every year (Unique structures I mean
less than 30% identical in sequence to proteins for which structures had
already been determined)
I could not find this data ın PDB . Is eventually
